ID I2QAG0_9BRAD Unreviewed; 615 AA.
AC I2QAG0;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Glutaminase {ECO:0000256|ARBA:ARBA00012918, ECO:0000256|HAMAP-Rule:MF_00313};
DE EC=3.5.1.2 {ECO:0000256|ARBA:ARBA00012918, ECO:0000256|HAMAP-Rule:MF_00313};
GN Name=glsA {ECO:0000256|HAMAP-Rule:MF_00313};
GN ORFNames=Bra1253DRAFT_01392 {ECO:0000313|EMBL:EIG56766.1};
OS Bradyrhizobium sp. WSM1253.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=319003 {ECO:0000313|EMBL:EIG56766.1, ECO:0000313|Proteomes:UP000005125};
RN [1] {ECO:0000313|EMBL:EIG56766.1, ECO:0000313|Proteomes:UP000005125}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM1253 {ECO:0000313|EMBL:EIG56766.1,
RC ECO:0000313|Proteomes:UP000005125};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Brau L., Yates R., O'Hara G., Rui T.,
RA Howieson J., Reeve W., Woyke T.;
RT "Improved High-Quality Draft sequence of Bradyrhizobium sp. WSM1253.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000005125}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM1253 {ECO:0000313|Proteomes:UP000005125};
RX PubMed=26629308;
RA Tiwari R., Howieson J., Yates R., Tian R., Held B., Tapia R., Han C.,
RA Seshadri R., Reddy T.B., Huntemann M., Pati A., Woyke T., Markowitz V.,
RA Ivanova N., Kyrpides N., Reeve W.;
RT "Genome sequence of Bradyrhizobium sp. WSM1253; a microsymbiont of
RT Ornithopus compressus from the Greek Island of Sifnos.";
RL Stand. Genomic Sci. 10:113-113(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamine = L-glutamate + NH4(+);
CC Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001062, ECO:0000256|HAMAP-
CC Rule:MF_00313};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881,
CC ECO:0000256|HAMAP-Rule:MF_00313}.
CC -!- SIMILARITY: Belongs to the glutaminase family.
CC {ECO:0000256|ARBA:ARBA00011076, ECO:0000256|HAMAP-Rule:MF_00313}.
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DR EMBL; JH600073; EIG56766.1; -; Genomic_DNA.
DR RefSeq; WP_007592301.1; NZ_JH600073.1.
DR AlphaFoldDB; I2QAG0; -.
DR eggNOG; COG2066; Bacteria.
DR eggNOG; COG2905; Bacteria.
DR HOGENOM; CLU_027932_3_1_5; -.
DR OrthoDB; 9788822at2; -.
DR Proteomes; UP000005125; Unassembled WGS sequence.
DR GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:InterPro.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR Gene3D; 3.30.750.24; STAS domain; 1.
DR HAMAP; MF_00313; Glutaminase; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR015868; Glutaminase.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR002645; STAS_dom.
DR InterPro; IPR036513; STAS_dom_sf.
DR NCBIfam; TIGR03814; Gln_ase; 1.
DR PANTHER; PTHR12544; GLUTAMINASE; 1.
DR PANTHER; PTHR12544:SF29; GLUTAMINASE; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF04960; Glutaminase; 1.
DR Pfam; PF01740; STAS; 1.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR SUPFAM; SSF52091; SpoIIaa-like; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS50801; STAS; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|HAMAP-Rule:MF_00313};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00313}.
FT DOMAIN 347..425
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
FT DOMAIN 482..597
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 126
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 201
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 253
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 271
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
SQ SEQUENCE 615 AA; 66988 MW; 4126F35E8773B383 CRC64;
MKQLSPLATA WTRSKPPLLR FLDNCLSEFS AETSGAVADY IPELGKADPA CFGISLATLD
GHVYEVGDSR APFTIQSMSK PFVFALALDL LGANRVESAI GVEPSGDPFN SIRLNSENHP
FNPMVNAGAI ACTGLIHDSK GTDAFEQIRL ALSRFAGRDL AVDEAVYASE SQTGDRNRAI
GYLLKTNAVI SDNVAAVLDV YFRQCAVLVT ARDIAVMAAT LANRGVNPVT GEQVLTPYAI
SRTLSVMTSS GMYDYAGEWI YRIGIPAKSG VGGGILAALP ARLGLGSYSP RLDKHGNSVR
GIKVCEALSS HYDLHMLNRS DDARNAVIAD YDIGKSPSRR VRRPQERDIL AAHEQEVRII
ELVGTLSLSA VDYVSRRLAG RPRPQFVIFD LHRVTSTTRA GARLVAEAFE ELAALNVTVV
LSGVRRASKE WDSLREWSAE LKNVRDFYLL DTAIEWAEDQ IIYRYGGSID FHETTELAEQ
PLLAGMSEEE LTDLASICTI RTYQSGTKIL TTGDPADALF FLRSGAVHVT LPDGVRLATL
TAGMAFGEMA LIETTRSADV FVDMAATAFE APLKAFERFR KQHPHASERI MRNLAQLLAD
RLIVANARVD ILTST
//
